[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. DOI=10.1021/bi00122a001; PubMed=1371399 [NCBI, ExPASy, EBI, Israel, Japan] Shiota S., von Wronski M.A., Tano K., Bigner D.D., Brent T.P., Mitra S.; "Characterization of cDNA encoding mouse DNA repair protein O6-methylguanine-DNA methyltransferase and high-level expression of the wild-type and mutant proteins in Escherichia coli."; Biochemistry 31:1897-1903(1992).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=C3H, and C57BL/6; TISSUE=Thymus; Shimada Y., Kakinuma S., Kubo A., Nishimura M.; "MGMT sequence of B6 and C3H mice."; Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N-3; TISSUE=Mammary gland; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

Comments

FUNCTION: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
CATALYTIC ACTIVITY: DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine.
COFACTOR: Binds 1 zinc ion (By similarity).
SUBCELLULAR LOCATION: Nucleus (Probable).
SIMILARITY: Belongs to the MGMT family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M84524; AAA37126.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB092489; BAC16763.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB092490; BAC16764.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031888; AAH31888.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A41809; A41809.

NP_032624.1; -.

3D structure databases

HSSP

P16455; 1EH7. [HSSP ENTRY / PDB]

P26187; 5-185.

PTM databases

P26187; -.

Organism-specific databases

MGI

MGI:96977; Mgmt.

Gene expression databases

ArrayExpress

P26187; -.

CleanEx

MM_MGMT; -.

GermOnline

ENSMUSG00000054612; Mus musculus.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003908;	Molecular function: methylated-DNA-[protein]-cysteine S-methyltransferase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006307;	Biological process: DNA dealkylation (inferred from direct assay from MGI).
GO:0043281;	Biological process: regulation of caspase activity (inferred from mutant phenotype from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR001497; MethylDNA_cys_MeTrfase_AS.
IPR014048; MethylDNA_cys_MeTrfase_DNA_bd.
IPR008332; MethylG_MeTrfase.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.

PANTHER

PTHR10815; MethylDNA_cys_mtrans_DNA_bd; 1.

Pfam

PF01035; DNA_binding_1; 1.
PF02870; Methyltransf_1N; 1.
Pfam graphical view of domain structure.

TIGR00589; ogt; 1.

PS00374; MGMT; 1.

Genome annotation databases

Ensembl

ENSMUSG00000054612; Mus musculus. [Contig view]

GeneID

17314; -.

KEGG

mmu:17314; -.

NMPDR

fig|10090.3.peg.17835; -.

Phylogenomic databases

HOGENOM

P26187; -.

HOVERGEN

P26187; -.

Other

NextBio

291876; -.

SOURCE

Mgmt; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; DNA damage; DNA repair; DNA-binding; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; Transferase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 211`	`210`	`Methylated-DNA--protein-cysteine methyltransferase.`	`PRO_0000139360`
`ACT_SITE`	`149 149`		`Nucleophile; methyl group acceptor (By similarity).`
`METAL`	`5 5`		`Zinc (By similarity).`
`METAL`	`24 24`		`Zinc (By similarity).`
`METAL`	`29 29`		`Zinc (By similarity).`
`METAL`	`89 89`		`Zinc (By similarity).`
`BINDING`	`99 99`		`DNA; via amide nitrogen (By similarity).`
`BINDING`	`118 118`		`DNA (By similarity).`
`BINDING`	`119 119`		`DNA; via amide nitrogen (By similarity).`
`BINDING`	`127 127`		`DNA (By similarity).`
`BINDING`	`132 132`		`DNA (By similarity).`
`BINDING`	`155 155`		`DNA; via amide nitrogen (By similarity).`
`MOD_RES`	`205 205`		`Phosphoserine (By similarity).`

Sequence information

Length: 211 AA [This is the length of the unprocessed precursor]

Molecular weight: 22435 Da [This is the MW of the unprocessed precursor]

CRC64: 838BB92B9A1083D6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAETCKMKYS VLDSPLGKME LSGCERGLHG IRLLSGKTPN TDPTEAPATP EVLGGPEGVP 

        70         80         90        100        110        120 
EPLVQCTAWL EAYFREPAAT EGLPLPALHH PVFQQDSFTR QVLWKLLKVV KFGETVSYQQ 

       130        140        150        160        170        180 
LAALAGNPKA ARAVGGAMRS NPVPILIPCH RVVRSDGAIG HYSGGGQAVK EWLLAHEGIP 

       190        200        210 
TGQPASKGLG LTGTWLKSSF ESTSSEPSGR N

P26187 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools